| pubmed-article:2536919 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2536919 | lifeskim:mentions | umls-concept:C0014644 | lld:lifeskim |
| pubmed-article:2536919 | lifeskim:mentions | umls-concept:C0029016 | lld:lifeskim |
| pubmed-article:2536919 | lifeskim:mentions | umls-concept:C0441635 | lld:lifeskim |
| pubmed-article:2536919 | lifeskim:mentions | umls-concept:C1510411 | lld:lifeskim |
| pubmed-article:2536919 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
| pubmed-article:2536919 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:2536919 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:2536919 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:2536919 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:2536919 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2536919 | pubmed:dateCreated | 1989-3-17 | lld:pubmed |
| pubmed-article:2536919 | pubmed:abstractText | The BNLF-1 gene from Epstein-Barr virus (EBV) induces anchorage-independent and tumorigenic growth in rodent cell lines. The BNLF-1 protein (also termed LMP) is a membrane protein, and its predicted amino acid sequence indicates that the protein has six membrane-spanning segments in addition to a short amino-terminal (approximately 25 amino acids) and a long carboxyl-terminal (approximately 200 amino acids) cytoplasmic domain. To identify the regions of the protein that are essential for its transforming activity, we have constructed deletion mutants of the BNLF-1 gene and tested them for transforming activity. Surprisingly, the entire carboxyl-terminal cytoplasmic domain is dispensable for transforming activity, whereas the putative membrane-spanning segments are essential. These observations indicate that BNLF-1 has a novel function that is distinct from the functions associated with other membrane-associated viral transforming proteins. We speculate that BNLF-1 is a receptor for a growth-promoting agent, with its trans-membrane domain involved in ligand binding, and its amino-terminal domain or cytoplasmic loops involved in coupling BNLF-1 to effector molecules in the cell, a situation analogous to the rhodopsin group of receptors. | lld:pubmed |
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| pubmed-article:2536919 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2536919 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2536919 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2536919 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:2536919 | pubmed:issn | 0950-9232 | lld:pubmed |
| pubmed-article:2536919 | pubmed:author | pubmed-author:SugdenBB | lld:pubmed |
| pubmed-article:2536919 | pubmed:author | pubmed-author:BaichwalV RVR | lld:pubmed |
| pubmed-article:2536919 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2536919 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:2536919 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2536919 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2536919 | pubmed:pagination | 67-74 | lld:pubmed |
| pubmed-article:2536919 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:2536919 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2536919 | pubmed:articleTitle | The multiple membrane-spanning segments of the BNLF-1 oncogene from Epstein-Barr virus are required for transformation. | lld:pubmed |
| pubmed-article:2536919 | pubmed:affiliation | McArdle Laboratory for Cancer Research, University of Wisconsin-Madison 53706. | lld:pubmed |
| pubmed-article:2536919 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2536919 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2536919 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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